DB code: S00157

CATH domain 2.60.130.10 : Protocatechuate 3,4-Dioxygenase, subunit A Catalytic domain
E.C. 1.13.11.1
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P07773 Catechol 1,2-dioxygenase
EC 1.13.11.1
1,2-CTD
YP_046127.1 (Protein)
NC_005966.1 (DNA/RNA sequence)
PF00775 (Dioxygenase_C)
PF04444 (Dioxygenase_N)
[Graphical View]

KEGG enzyme name
catechol 1,2-dioxygenase
catechol-oxygen 1,2-oxidoreductase
1,2-pyrocatechase
catechase
catechol 1,2-oxygenase
catechol dioxygenase
pyrocatechase
pyrocatechol 1,2-dioxygenase
CD I
CD II

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P07773 CATA_ACIAD Catechol + O(2) = cis,cis-muconate. Homodimer. Binds 1 Fe(3+) ion per subunit.

KEGG Pathways
Map code Pathways E.C.
MAP00361 gamma-Hexachlorocyclohexane degradation
MAP00362 Benzoate degradation via hydroxylation
MAP00364 Fluorobenzoate degradation
MAP00622 Toluene and xylene degradation
MAP00627 1,4-Dichlorobenzene degradation
MAP00629 Carbazole degradation

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00023 C00090 C00007 C02480
E.C.
Compound Iron Catechol O2 cis,cis-Muconate
Type heavy metal aromatic ring (only carbon atom) others carboxyl group
ChEBI 18248
82664
18248
82664
18135
18135
15379
26689
27140
15379
26689
27140
16508
16508
PubChem 23925
23925
289
289
977
977
5280518
5280518
1dlmA Bound:_FE Unbound Unbound Unbound
1dlmB Bound:_FE Unbound Unbound Unbound
1dlqA Bound:_FE Unbound Unbound Unbound
1dlqB Bound:_FE Unbound Unbound Unbound
1dltA Bound:_FE Bound:CAQ Unbound Unbound
1dltB Bound:_FE Bound:CAQ Unbound Unbound
1dmhA Bound:_FE Analogue:MCT Unbound Unbound
1dmhB Bound:_FE Analogue:MCT Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [14]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1dlmA TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dlmB TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dlqA TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dlqB TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dltA TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dltB TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dmhA TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)
1dmhB TYR 200;ARG 221 TYR 164;TYR 200;HIS 224;HIS 226(Fe binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.12, p.8471
[4]
Fig.7
[10]
Fig.3, Fig.4, p.95-96 6
[14]
Fig.6, p.436 1
[15]
p.3187-3189, Scheme 4
[17]
Scheme 1, p.8291-8293 1

References
[1]
Resource
Comments
Medline ID
PubMed ID 238971
Journal J Biol Chem
Year 1975
Volume 250
Pages 4848-55
Authors Fujiwara M, Golovleva LA, Saeki Y, Nozaki M, Hayaishi O
Title Extradiol cleavage of 3-substituted catechols by an intradiol dioxygenase, pyrocatechase, from a Pseudomonad.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 6773944
Journal J Biol Chem
Year 1980
Volume 255
Pages 8465-71
Authors Saeki Y, Nozaki M, Senoh S
Title Cleavage of pyrogallol by non-heme iron-containing dioxygenases.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 3015028
Journal Arch Biochem Biophys
Year 1986
Volume 248
Pages 130-7
Authors Pascal RA Jr, Huang DS
Title Reactions of 3-ethylcatechol and 3-(methylthio)catechol with catechol dioxygenases.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 3365096
Journal Arch Microbiol
Year 1988
Volume 149
Pages 188-97
Authors Engesser KH, Cain RB, Knackmuss HJ
Title Bacterial metabolism of side chain fluorinated aromatics: cometabolism of 3-trifluoromethyl(TFM)-benzoate by Pseudomonas putida (arvilla) mt-2 and Rhodococcus rubropertinctus N657.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 2394680
Journal J Bacteriol
Year 1990
Volume 172
Pages 5119-29
Authors Schlomann M, Fischer P, Schmidt E, Knackmuss HJ
Title Enzymatic formation, stability, and spontaneous reactions of 4-fluoromuconolactone, a metabolite of the bacterial degradation of 4-fluorobenzoate.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 1649626
Journal Biochemistry
Year 1991
Volume 30
Pages 7349-58
Authors Broderick JB, O'Halloran TV
Title Overproduction, purification, and characterization of chlorocatechol dioxygenase, a non-heme iron dioxygenase with broad substrate tolerance.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 8107120
Journal J Mol Biol
Year 1994
Volume 236
Pages 377-8
Authors Earhart CA, Hall MD, Michaud-Soret I, Que L Jr, Ohlendorf DH
Title Crystallization of catechol-1,2 dioxygenase from Pseudomonas arvilla C-1.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 9369233
Journal FEBS Lett
Year 1997
Volume 416
Pages 61-4
Authors Briganti F, Pessione E, Giunta C, Scozzafava A
Title Purification, biochemical properties and substrate specificity of a catechol 1,2-dioxygenase from a phenol degrading Acinetobacter radioresistens.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 9677336
Journal Biochem J
Year 1998
Volume 333
Pages 741-7
Authors Strachan PD, Freer AA, Fewson CA
Title Purification and characterization of catechol 1,2-dioxygenase from Rhodococcus rhodochrous NCIMB 13259 and cloning and sequencing of its catA gene.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 9799107
Journal Eur J Biochem
Year 1998
Volume 257
Pages 92-100
Authors Ridder L, Briganti F, Boersma MG, Boeren S, Vis EH, Scozzafava A, Veeger C, Rietjens IM
Title Quantitative structure/activity relationship for the rate of conversion of C4-substituted catechols by catechol-1,2-dioxygenase from Pseudomonas putida (arvilla) C1.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 10515940
Journal J Bacteriol
Year 1999
Volume 181
Pages 6478-87
Authors D'Argenio DA, Vetting MW, Ohlendorf DH, Ornston LN
Title Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 10438749
Journal J Bacteriol
Year 1999
Volume 181
Pages 4812-7
Authors Riegert U, Heiss G, Kuhm AE, Muller C, Contzen M, Knackmuss HJ, Stolz A
Title Catalytic properties of the 3-chlorocatechol-oxidizing 2, 3-dihydroxybiphenyl 1,2-dioxygenase from Sphingomonas sp. strain BN6.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11307956
Journal J Protein Chem
Year 2000
Volume 19
Pages 709-16
Authors Briganti F, Pessione E, Giunta C, Mazzoli R, Scozzafava A
Title Purification and catalytic properties of two catechol 1,2-dioxygenase isozymes from benzoate-grown cells of Acinetobacter radioresistens.
Related PDB
Related UniProtKB
[14]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10801478
Journal Structure Fold Des
Year 2000
Volume 8
Pages 429-40
Authors Vetting MW, Ohlendorf DH
Title The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker.
Related PDB 1dlm 1dlq 1dlt 1dmh
Related UniProtKB P07773
[15]
Resource
Comments
Medline ID
PubMed ID 11399191
Journal Inorg Chem
Year 2001
Volume 40
Pages 3181-90
Authors Jo DH, Chiou YM, Que L Jr
Title Models for extradiol cleaving catechol dioxygenases: syntheses, structures, and reactivities of iron(II)-monoanionic catecholate complexes.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 12450835
Journal Appl Environ Microbiol
Year 2002
Volume 68
Pages 6114-20
Authors Haroune N, Combourieu B, Besse P, Sancelme M, Reemtsma T, Kloepfer A, Diab A, Knapp JS, Baumberg S, Delort AM
Title Benzothiazole degradation by Rhodococcus pyridinovorans strain PA: evidence of a catechol 1,2-dioxygenase activity.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 14658880
Journal Inorg Chem
Year 2003
Volume 42
Pages 8283-93
Authors Velusamy M, Palaniandavar M, Gopalan RS, Kulkarni GU
Title Novel iron(III) complexes of tripodal and linear tetradentate bis(phenolate) ligands: close relevance to intradiol-cleaving catechol dioxygenases.
Related PDB
Related UniProtKB

Comments

Created Updated
2004-07-07 2009-03-19